MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint anonymous-2014t-1 Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential in vitro In vitro ms interact detect detection by mass spectrometry ms interact detect predetermined predetermined participant predetermined rozovsky@udel.edu 2014 imex curation Liu J., Zhang Z., Rozovsky S. FEBS Lett. (0014-5793) Only protein-protein interactions anonymous-2014x-2 Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential in vitro In vitro comigration in sds comigration in sds page comigration in sds weight by comassie molecular weight estimation by coomasie staining weight by comassie rozovsky@udel.edu 2014 imex curation Liu J., Zhang Z., Rozovsky S. FEBS Lett. (0014-5793) Only protein-protein interactions selk_human Selenoprotein K SELENOK SELK HSPC030 HSPC297 protein protein human Homo sapiens Human MVYISNGQVLDSRSQSPWRLSLITDFFWGIAEFVVLFFKTLLQQDVKKRRSYGNSSDSRYDDGRGPPGNPPRRMGRINHLRGPSPPPMAGGUGR selk 1562264 n/a SelK 1562266 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified strep tag strep tag strep tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 2.0 direct interaction direct interaction false false false f2b Furthermore, when examined by electrospray mass spectrometry, SelK U92 ionized as a dimer under non-reducing conditions (Fig. 2B). selk-1 1562265 n/a SelK 1562266 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified strep tag strep tag strep tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false undefined mutation mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 2.0 direct interaction direct interaction false false false f2a sf1 As can be observed from a SDS-PAGE run under non-reducing conditions (Fig. 2A), SelK U92 migrated as a dimer of 23 kDa, SelK U92C migrated mostly as a dimer, and SelK U92S migrated mostly as a monomer. All three proteins migrated as a monomer of 11.5 kDa under reducing conditions. The dimerization is not exclusively dependent on the presence of a diselenide bond since SelK U92S, which has no intermolecular bond, can run as both a monomer and dimer on denaturing SDS-PAGE when its concentration is sufficiently high (Supplementary data, Fig. S1).